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CacyBP expression is regulated by E2F1, EGR1, and CREB transcription factors in colorectal cancer HCT116 cells.
Results suggest that CacyBP/SIP plays an important role in inhibiting glioma cell migration and invasion through promoting the degradation of cytoplasmic p27.
Data show that S100 calcium binding protein A6 (S100A6) is required for the Ca2+-dependent nuclear translocation of calcyclin binding protein (CacyBP/SIP) in colon cancer SW480 cells.
CacyBP/SIP nuclear localization, dependent on S100 protein, suppresses gastric cancer tumorigenesis through beta-catenin degradation and the dephosphorylation of ERK1/2 during the G2 phase.
Our data have shown for the first time the regulation of CacyBP/SIP gene expression by NFAT1. Since NFAT transcription factors are involved in processes related to immune response, these results indicate potential involvement of CacyBP/SIP in the immune system.
These results suggest that CacyBP/SIP may be promoting growth of colon cancer cells by enhancing ubiquitin-mediated degradation of p27kip1.
The biological characteristics and target proteins of CacyBP/SIP and its exact role in various cancers are discussed. Review.
CacyBP/SIP nuclear translocation contributes to the proliferation of gastric cancer cells, and CacyBP/SIP exerts this effect, at least in part, by stimulating ubiquitin-mediated degradation of p27Kip1.
CacyBP/SIP plays an important role in inhibiting apoptosis of glioma cells which might be mediated by ERK1/2 signaling pathway.
CacyBP/SIP is a useful indicator of dis processes in Chronic Lymphocytic Leukemia (CLL) and plays an important role in sustaining the balance of cell proliferation and apoptosis.
CacyBP/SIP nuclear translocation promotes the proliferation and cell cycle progression of gastric cancer cells.
Overexpression of CacyBP is associated with glioma.
This study presents CacyBP as a promising candidate biomarker for colorectal cancer (CRC) metastasis and also sheds light on the underlying molecular mechanism by which CacyBP promotes CRC metastasis.
CacyBP enhances multidrug resistance of pancreatic cancer cells by regulation of P-gp and Bcl-2.
These findings reveal a novel function for SNRK in the regulation of colon cancer cell proliferation and beta-catenin signaling.
different activity of CacyBP/SIP in neuroblastoma NB2a and colon cancer HCT116 cells might affect the ERK1/2 pathway in the differentiation or proliferation processes
new insight into the interaction between S100 proteins and CacyBP/SIP
Data show that CacyBP/SIP might develop into another possible therapeutic target.
Poor cellular differentiation, lymph node invasion, and clinicopathological staging in breast cancer were associated with CacyBP/SIP expression.
CacyBP/SIP exhibits a phosphatase activity toward ERK1/2 kinases while its E217K mutant does not.
involvement of CacyBP/SIP in the regulation of p38 kinase activity, in addition to that of ERK1/2, might point to the function of CacyBP/SIP in pro-survival and pro-apoptotic pathways.
In undifferentiated and differentiated tumor cells, CacyBP level has an effect on the ERK1/2-CREB-BDNF pathway.
Calcyclin-binding protein/Siah-1-interacting protein (CacyBP/SIP) was initially described as a binding partner of S100A6 in the Ehrlich ascites tumor cells and later as a Siah-1-interacting protein. Its role has been studied in various mouse tumors and cell lines. Review.
sumoylated CacyBP/SIP is present in the cytoplasmic and not in the nuclear fraction. We have also established that lysine 16 is the residue which undergoes sumoylation in the CacyBP/SIP protein.
SIP (-/-) embryonic fibroblasts have increased levels of cytosolic p27 and exhibit increased cell motility compared to wild-type cells.
Cacybp is associated with acute lung injury
Data indicated that CacyBP/SIP could simultaneously interact with tubulin and actin, suggesting that CacyBP/SIP might link actin and tubulin cytoskeletons.
binds EF-hand proteins of the S100 family [CacyBP/SIP]
Structural details of multiple sites of protein-protein interactions on SIP provide insight into the mechanism that drives the formation of the Siah-1 E3 ubiquitin ligase complex [SIP]
SIP (CacyBP)-thymocytes have an impaired pre-TCR checkpoint with failure of TCRbeta gene rearrangement and increased apoptosis, resulting in reduced cellularity of the thymus.
The results show the changing localization and levels of beta-catenin in the mouse uterus during decidualization and suggest potential roles for the BTRC and CACYBP E3 ligase mechanisms of beta-catenin ubiquitination in the uterus during decidualization.
These results suggest that CacyBP/SIP, via its interaction with tubulin, might contribute to the differentiation of neuroblastoma NB2a cells.
These data suggest that the binding of CacyBP/SIP with ERK1/2 might regulate Elk-1 phosphorylation/transcriptional activity and that S100A6 might further modulate this effect via Ca(2+)-dependent interaction with CacyBP/SIP and competition with ERK1/2.
The protein encoded by this gene is a calcyclin binding protein. It may be involved in calcium-dependent ubiquitination and subsequent proteosomal degradation of target proteins. It probably serves as a molecular bridge in ubiquitin E3 complexes and participates in the ubiquitin-mediated degradation of beta-catenin. Two alternatively spliced transcript variants encoding different isoforms have been found for this gene.
, calcyclin binding protein
, Calcyclin binding protein
, S100A6-binding protein
, Siah-interacting protein (SIP)
, growth-inhibiting gene 5 protein
, siah-interacting protein